Self-compartmentalizing proteases

Andrei Lupas, John M. Flanagan, Tomohiro Tamura, Wolfgang Baumeister

Research output: Contribution to journalReview article

197 Citations (Scopus)

Abstract

Among the hundreds of proteases characterized so far, most of which are monomeric or dimeric, there is a small group that form compartments through self-association and that segregate their proteolytic active sites to the interior of these compartments. Although few in number, they represent the main agents of intracellular protein breakdown. They belong to different hydrolase families but have converged towards the same barrel-shaped architecture. Frequently, they are coupled to chaperone-like ATPases of similar quaternary structure that regulate the access to the proteolytic compartments and appear to have been recruited from the same branch of P-loop NTPases.

Original languageEnglish (US)
Pages (from-to)399-404
Number of pages6
JournalTrends in Biochemical Sciences
Volume22
Issue number10
DOIs
StatePublished - Oct 1 1997

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Hydrolases
Adenosine Triphosphatases
Catalytic Domain
Peptide Hydrolases
Proteins
protease So

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Lupas, Andrei ; Flanagan, John M. ; Tamura, Tomohiro ; Baumeister, Wolfgang. / Self-compartmentalizing proteases. In: Trends in Biochemical Sciences. 1997 ; Vol. 22, No. 10. pp. 399-404.
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Self-compartmentalizing proteases. / Lupas, Andrei; Flanagan, John M.; Tamura, Tomohiro; Baumeister, Wolfgang.

In: Trends in Biochemical Sciences, Vol. 22, No. 10, 01.10.1997, p. 399-404.

Research output: Contribution to journalReview article

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AU - Lupas, Andrei

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AU - Tamura, Tomohiro

AU - Baumeister, Wolfgang

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